Gammeltoft S, Kowalski A, Fehlmann M, van Obberghen E
FEBS Lett. 1984 Jun 25;172(1):87-90. doi: 10.1016/0014-5793(84)80879-0.
In rat brain cortex synaptosomes insulin stimulated the phosphorylation of its own receptor beta-subunit (94 kDa) as identified by immunoprecipitation with anti-insulin or anti-receptor antiserum. The receptor alpha-subunit (115 kDa) was characterized by specific labeling with 125I-labeled photoreactive insulin. These observations indicate that: (i) insulin receptors in brain are composed of alpha-subunits which bind insulin, and beta-subunits, the phosphorylation of which can be stimulated by insulin; (ii) the size of alpha-subunits in brain is significantly smaller than in other tissues (115 vs 130 kDa), whereas beta-subunits (94 kDa) are identical. We suggest that brain insulin receptors represent a subtype regarding their binding function, whereas their enzyme function is more conserved.
在大鼠脑皮质突触体中,胰岛素可刺激其自身受体β亚基(94 kDa)的磷酸化,这是通过用抗胰岛素或抗受体抗血清进行免疫沉淀鉴定得出的。受体α亚基(115 kDa)通过用125I标记的光反应性胰岛素进行特异性标记来表征。这些观察结果表明:(i)脑中的胰岛素受体由结合胰岛素的α亚基和其磷酸化可被胰岛素刺激的β亚基组成;(ii)脑中α亚基的大小明显小于其他组织(115 kDa对130 kDa),而β亚基(94 kDa)是相同的。我们认为,脑胰岛素受体在其结合功能方面代表一种亚型,而其酶功能则更具保守性。